Angiotensin I‐converting enzyme inhibitory peptides FQPSF and LKYPI identified in Bacillus subtilis A26 hydrolysate of thornback ray muscle

Abstract

Summary Angiotensin I‐converting enzyme (ACE) inhibitory peptides have been searched in thornback ray (Raja clavata) muscle hydrolysed with Bacillus subtilis A26 proteases until a hydrolysis degree of 18.35%. The hydrolysate showed an IC50 of 0.83 mg mL−1. To identify peptides responsible for this activity, the extract was eluted through size‐exclusion chromatography and fractions collected. The highest ACE inhibitory activity was found for fractions F2 and F3 which had IC50 of 0.42 and 0.51 mg mL−1, respectively. These fractions were analysed by nano‐liquid chromatography coupled to tandem mass spectrometry (nLC‐MS/MS). A total of 131 and 108 peptide sequences mainly derived from actin, myosin heavy chain and procollagen alpha 1 chain proteins were identified in fractions F2 and F3, respectively. FQPSF and LKYPI showed the best results with an IC50 of 12.56 and 27.07 μM, respectively. These results prove the potential of thornback ray muscle hydrolysate as a source of ACE inhibitory peptides.

In silico analysis and antihypertensive effect of ACE-inhibitory peptides from smooth-hound viscera protein hydrolysate: Enzyme-peptide interaction study using molecular docking simulation

“…Interestingly, all peptides were found novelty identified when compared to previously reported ACE-inhibitory peptides available in the literature. peptides with high ACE-inhibitory capacity [8,38]. Furthermore, actin-derived peptides were found at a percentage of 12 and 10% in SF1 (Fig.…”

“…Previous study have shown that ACE-inhibitory peptides from thornback ray muscle hydrolysates were mainly derived from actin (more than 47%) [8].…”

Protective effects of thornback ray muscle protein hydrolysate against dyslipidemia, oxidative stress and reduced fertility induced by high cholesterol diet in adult male rats

“…Effectively, several researchers groups, have been able to generate various biological activities from different marine proteins in vitro [7][8][9] and in vivo.…”

Controlled enzymatic hydrolysis of pollen protein as promising tool for production of potential bioactive peptides

“…ACE‐inhibitory peptides can attach to ACE active site or inhibitor site, which can modify the protein confirmation and prevent from Angiotensin binding to the ACE active site (Wijesekara & Kim, ). Hydrophilic peptides cannot access the active site of ACE (Lassoued et al, ). Considering DPPH scavenging activity of PHP (fractions 62–64 of SEC), fraction eluting at 37 and 32 min showed the highest activity (90.89 and 89.72%).…”

“…Hydrophilic peptides cannot access the active site of ACE (Lassoued et al, 2016). Considering DPPH scavenging activity of PHP (fractions 62-64 of SEC), fraction eluting at 37 and 32 min showed the highest activity (90.89 and 89.72%).…”